Information on EC 1.1.1.138 - mannitol 2-dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.1.1.138
-
RECOMMENDED NAME
GeneOntology No.
mannitol 2-dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-mannitol + NADP+ = D-fructose + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
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SYSTEMATIC NAME
IUBMB Comments
D-mannitol:NADP+ 2-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-68-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain A5
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain HH-01, KCCM-10252
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Manually annotated by BRENDA team
Cenococcum graniforme
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-
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Manually annotated by BRENDA team
Ceratocystis multiannulata
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-
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Manually annotated by BRENDA team
Diplodia viticola Desm.
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-
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Manually annotated by BRENDA team
strain IFO 12528
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Manually annotated by BRENDA team
NRRL B-3693, enzyme production depends on growth on fructose or sucrose
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Manually annotated by BRENDA team
strain ATCC 53608, gene mdh
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain QM9414 (ATCC 26921), synonym Trichoderma reesei
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Manually annotated by BRENDA team
strain QM9414 (ATCC 26921), synonym Trichoderma reesei
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Manually annotated by BRENDA team
plant symbiotic ascomycete fungus, strain MYA-1019
UniProt
Manually annotated by BRENDA team
biotrophic plant pathogenic rust fungus, gene MAD1
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-deoxy-6-methyl-D-glucitol + NADP+
1-deoxy-6-methyl-D-glucose + NADPH
show the reaction diagram
-
poorer substrate than D-glucitol
-
?
1-deoxy-6-methyl-D-mannitol + NADP+
1-deoxy-6-methyl-D-fructose + NADPH
show the reaction diagram
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poorer substrate than D-mannitol
-
?
1-deoxy-D-glucitol + NADP+
1-deoxy-D-glucose + NADPH
show the reaction diagram
-
poorer substrate than glucitol
-
?
1-deoxy-D-mannitol + NADP+
1-deoxy-D-fructose + NADPH
show the reaction diagram
-
poorer substrate than D-mannitol
-
?
arabinose + NADPH + H+
arabinitol + NADP+
show the reaction diagram
-
-
-
-
r
D-arabinitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
D-fructose + NADPH
D-mannitol + NADP+
show the reaction diagram
D-fructose + NADPH + H+
D-mannitol + NADP+
show the reaction diagram
D-mannitol + 3-acetylpyridine adenine dinucleotide phosphate
D-fructose + 3-acetylpyridine adenine dinucleotide phosphate(H)
show the reaction diagram
-
7.5% of the activity compared to NADP+
-
?
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
show the reaction diagram
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-mannitol + NADP+
D-fructose + NADPH + H+
show the reaction diagram
D-mannitol + thio-NADP+
D-fructose + thio-NADPH
show the reaction diagram
-
30% of the activity compared to NADP+
-
?
D-mannose + NADPH + H+
D-mannitol + NADP+
show the reaction diagram
-
-
-
-
r
D-sorbitol + NADP+
D-sorbose + NADPH + H+
show the reaction diagram
L-arabinitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
L-sorbitol + NADP+
L-sorbose + NADPH
show the reaction diagram
L-sorbitol + NADP+
L-sorbose + NADPH + H+
show the reaction diagram
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21% of the activity with D-mannitol
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-
r
perseitol + NADP+
? + NADPH
show the reaction diagram
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6% of the activity compared to D-mannitol
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?
ribose + NADPH + H+
ribitol + NADP+
show the reaction diagram
-
-
-
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r
xylose + NADPH + H+
xylitol + NADP+
show the reaction diagram
-
-
-
-
r
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose + NADPH
D-mannitol + NADP+
show the reaction diagram
D-mannitol + NAD(P)+
D-fructose + NAD(P)H + H+
show the reaction diagram
-
-
-
-
r
D-mannitol + NADP+
D-fructose + NADPH + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)+
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NADP+ is the preferred cofactor in the forward reaction
NAD(P)H
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NADPH is the preferred cofactor in the reverse reaction
NAD+
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5-10% of the activity with NADP+
NADH
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5-10% of the activity with NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
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37% activation at 5 mM only in D-mannitol oxidation
Ca2+
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52% activation at 5 mM up to 140% at 10 mM only in D-mannitol oxidation
Cu2+
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increases the intracellular activity of mannitol dehydrogenase 1.6fold
Mn2+
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15% activation at 5 mM only in D-mannitol oxidation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
inhibits 96% at 4 mM, reduction reaction
2-mercaptoethanol
Ca2+
inhibits 21% at 1 mM, reduction reaction
D-fructose
D-mannitol
dithiothreitol
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0.5 mM, complete inhibition
DTT
inhibits 89% at 0.5 mM, reduction reaction
Fe2+
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86% inhibition at 1 mM
glutathione
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0.5 mM, complete inhibition
KCl
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half Vmax/Km at less than 0.1 M due to general ionic strength effect
KNO3
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half Vmax/Km at less than 0.1 M due to general ionic strength effect
L-cysteine
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0.5 mM, complete inhibition
Mg2+
inhibits 19% at 1 mM, reduction reaction
NaCl
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half Vmax/Km at less than 0.1 M due to general ionic strength effect
NADP+
NADPH
p-chloromercuribenzoate
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0.2 mM, complete inhibition
Sn2+
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29% inhibition at 1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
activates 5% at 5 mM, reduction reaction
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
385
arabinose
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pH 7.5, 37C
190
D-arabinitol
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0.804 - 1200
D-fructose
560
D-glucitol
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-
0.46 - 680
D-mannitol
352
D-mannose
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pH 7.5, 37C
9
NAD+
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pH 6.2, 37C, recombinant enzyme
0.24 - 0.612
NADH
0.014 - 0.35
NADP+
0.00525 - 0.1
NADPH
212
ribose
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pH 7.5, 37C
402
xylose
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pH 7.5, 37C
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0011
Cu2+
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pH 7.5, 37C
183
D-mannitol
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pH 7.5, 37C
188
mannitol
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pH 7.5, 37C
0.18 - 0.21
NADP+
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.4
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recombinant enzyme, forward reaction
0.5 - 0.9
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crude enzyme extract, optimization of culture conditions, overview
0.54
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pH 9.0, 30C
0.61
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crude recombinant Escherichia coli cell extract
1
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recombinant enzyme, reverse reaction
3.1
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substrate D-fructose + NADH, pH 7.5, 37C
3.2
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substrate arabinose, pH 7.5, 37C
5.1
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substrate xylose, pH 7.5, 37C
5.2
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substrate ribose, pH 7.5, 37C
6.1
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substrate D-mannose, pH 7.5, 37C
9.1
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substrate D-mannitol, pH 7.5, 37C
124.6
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purified recombinant enzyme
277
purified native enzyme
315
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substrate D-fructose + NADPH, pH 7.5, 37C
331
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pH 5.5, 30C
350
purified native enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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reverse reaction, recombinant enzyme
5.5
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reduction of D-fructose
6 - 8
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reduction of D-fructose
6
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reverse reaction, recombinant enzyme
6.2
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forward reaction, recombinant enzyme
7.3
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50 mM MOPS-KOH buffer
7.5 - 8
reduction reaction
7.8
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assay at
7.9 - 8.1
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D-fructose reduction
7.9 - 8.3
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D-mannitol oxidation
8
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assay at, both reaction directions
8.7 - 8.8
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D-mannitol oxidation
9
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D-mannitol oxidation
9 - 10
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oxidation of D-mannitol
9
oxidation reaction
10
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oxidation of fructose
10.25
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D-mannitol oxidation
10.5
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forward reaction, recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
reduction of D-fructose, 35% of maximum activity
5 - 7
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reverse reaction, 81% of maximal activity at pH 5.0, 22% at pH 7.0, 72% at pH 5.6, and 60% at pH 7.4
6 - 9.5
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95% of its maximal activity for 5 min
6.5
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reduction of D-fructose, 50% of maximum activity
8.5 - 11
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sharp decline below pH 8.5 and above pH 11.0, forward reaction, recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature, forward reaction
25
-
assay at, both reaction directions
35
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reduction of D-fructose
37 - 40
both reaction directions
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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reduction of D-fructose, 44% of maximum activity
60
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reduction of D-fructose, 15% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
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4 * 28000, electrospray mass spectroscopy
28500
monomer, blue native gel electrophoresis
29500
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4 * 29500, SDS-PAGE
32000
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4 * 32000, SDS-PAGE
34500
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2 * 43000 + 2 * 34500, SDS-PAGE, both subunits have the same amino-terminal amino acid sequence
35000
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4 * 35000, SDS-PAGE
36400
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PAGE
37279
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2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 37279, recombinant His6-tagged enzyme, mass spectrometry
38000
4 * 38000, SDS-PAGE, peptide mapping
43000
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2 * 43000 + 2 * 34500, SDS-PAGE, both subunits have the same amino-terminal amino acid sequence
50000
-
gel filtration
75000
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recombinant enzyme, gel filtration
110000
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gel filtration
112000
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dynamic light scattering
114000
tetramer, blue native gel electrophoresis
115000 - 130000
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gel filtration, rate zonal ultracentrifugation
140000
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gel filtration
142000
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gel filtration
160000
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gel filtration
163000
gel filtration
170000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 29000, SDS-PAGE
heterotetramer
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2 * 43000 + 2 * 34500, SDS-PAGE, both subunits have the same amino-terminal amino acid sequence
monomer
tetramer
additional information
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structure-function analysis of enzyme and the family of polyol-specific long-chain dehydrogenases/reductases. G33 is in the N-terminal coenzyme-binding domain, D230 and K295 are at an interdomain segment contributing to the active site in which K295 likely functions as the catalytic general acid/base
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 1.8-2.8 A resolution
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binary complex with NADP+; binary complex with NADP+ at 1.5 A resolution, catalytic triad is assigned to Ser149, Tyr169 and Lys173
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crystal structures of Cladosporium herbarum MtDH in two different conformations is determined
ammonium sulfate precipitation
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 9.5
-
stable within
285855
4.5 - 8
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-
655118
6
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50 mM MOPS-KOH buffer, after an initial loss of 25% of activity stable for 5 days at 30C
285860
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
50 mM MOPS-KOH buffer, pH 6.0, stable for 5 days
35
-
stable up to
53
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20-50% retaining activity after 20 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM Tris-HCl, pH 7.5, 10 mM 2-mercaptoethanol, 0.05 mM PMSF, 50%, v/v, glycerol, 1 month
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-80C, 50 mM MOPS, pH 7.5, 1 mM DTT, 50 mM NaCl, several weeks
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4C, no loss of activity within 1 month
Diplodia viticola Desm.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 13.4fold by ammonium sulfate fractionation, hydrophobic interaction chromatography, and anion exchange chromatography; purified by standard chromatographic methods
native enzyme from mycelia 368fold by anion exchange chromatography, ultrafiltration, and 2',5'-ADP affinity chromatography
partial
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultratfiltration
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to crystalline state, chromatography techniques, crystallization
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to homogeneity, affinity chromatography
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to homogeneity, chromatography techniques
to homogeneity, chromatography techniques, affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, the enzyme shows a carbon responsive transcriptional pattern and is up-regulated when mycelia are transferred to a culture medium containing D-mannitol or D-fructose, quantitative expression and phylogenetic analysis
expressed in E. coli; gene MtDH, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli
expression in Escherichia coli
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expression in Pichia pastoris, gene cloning in Escherichia coli
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expression of mutant enzymes in Escherichia coli strain JM109
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gene MAD1, expression analysis in fungal tissue, recombinant expression in yeast
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gene mdh, DNA and amino acid sequence determination and compiational amnipulation, expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D69A
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site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, cf. EC 1.1.1.67, which is switched to NADP(H), NADP(H) is equally utilized as NAD(H)
E68K
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site-directed mutagenesis, the mutant shows an altered cofactor specificity compared to the wild-type enzyme, cf. EC 1.1.1.67, which is switched to NADP(H), NADP(H) is preferred by 10fold over NAD(H)
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
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optimization of culture conditions for production of mannitol, best conditions give 213 g/l mannitol from 250 g/l fructose
synthesis